MMP9 gene

The MMP9 gene (MMP3 stands for: Matrix Metallopeptidase 9) is a protein-coding gene located on chromosome 20q13.12.

Proteins of the matrix metalloproteinase (MMP) family are involved in the degradation of the extracellular matrix in normal physiological processes such as embryonic development, reproduction and tissue remodeling as well as in disease processes such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys indicate that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from the bone marrow, and studies in mice suggest a role in tumor-associated tissue remodeling.

Diseases associated with MMP9 include metaphyseal anadysplasia 2.

Matrix metalloproteinases (MMPs), also known as matrixins, are zinc-dependent endopeptidases and the most important proteases in ECM degradation. MMPs are able to degrade various extracellular molecules and a number of bioactive molecules.

Matrix metalloproteinase-9 plays an essential role in the local proteolysis of the extracellular matrix and in leukocyte migration (Wilhelm SM et al. 1989). MMP-9 protease may play a role in osteoclastic resorption of bone. Cleaves type IV and type V collagen into large C-terminal three-quarter fragments and shorter N-terminal one-quarter fragments (Tschesche H et al. 1992) Degrades fibronectin, but not laminin or Pz peptide.

1. Nagase H et al. (1990) Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry 29:5783-5789.
2. Tschesche H et al. 1992) Latent collagenase and gelatinase from human neutrophils and their activation. Matrix Suppl 1:245-55.).
3. Wilhelm SM et al. (1989) SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem 264:17213-219.